ID PURK_VIBPA Reviewed; 377 AA.
AC Q87KE0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 13-FEB-2019, entry version 94.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000255|HAMAP-Rule:MF_01928};
DE Short=N5-CAIR synthase {ECO:0000255|HAMAP-Rule:MF_01928};
DE EC=6.3.4.18 {ECO:0000255|HAMAP-Rule:MF_01928};
DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_01928};
GN Name=purK {ECO:0000255|HAMAP-Rule:MF_01928}; OrderedLocusNames=VP3037;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-
CC aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-
CC carboxyaminoimidazole ribonucleotide (N5-CAIR).
CC {ECO:0000255|HAMAP-Rule:MF_01928}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP +
CC hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-
CC ribosyl)imidazole + ADP + 2 H(+) + phosphate;
CC Xref=Rhea:RHEA:19317, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58730,
CC ChEBI:CHEBI:137981, ChEBI:CHEBI:456216; EC=6.3.4.18;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01928};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_01928}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01928}.
CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
CC Rule:MF_01928}.
DR EMBL; BA000031; BAC61300.1; -; Genomic_DNA.
DR RefSeq; NP_799416.1; NC_004603.1.
DR RefSeq; WP_005461432.1; NC_004603.1.
DR ProteinModelPortal; Q87KE0; -.
DR SMR; Q87KE0; -.
DR STRING; 223926.VP3037; -.
DR EnsemblBacteria; BAC61300; BAC61300; BAC61300.
DR GeneID; 1190636; -.
DR KEGG; vpa:VP3037; -.
DR PATRIC; fig|223926.6.peg.2921; -.
DR eggNOG; ENOG4105CY8; Bacteria.
DR eggNOG; COG0026; LUCA.
DR HOGENOM; HOG000034026; -.
DR KO; K01589; -.
DR OMA; APRTHNS; -.
DR BioCyc; VPAR223926:G1GTB-3179-MONOMER; -.
DR UniPathway; UPA00074; UER00942.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:InterPro.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1490.20; -; 1.
DR HAMAP; MF_01928; PurK; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR005875; PurK.
DR InterPro; IPR040686; PurK_C.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR Pfam; PF02222; ATP-grasp; 1.
DR Pfam; PF17769; PurK_C; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01161; purK; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1 377 N5-carboxyaminoimidazole ribonucleotide
FT synthase.
FT /FTId=PRO_0000075017.
FT DOMAIN 97 287 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_01928}.
FT NP_BIND 138 144 ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT NP_BIND 175 178 ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT NP_BIND 257 258 ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT BINDING 93 93 ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT BINDING 133 133 ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT BINDING 183 183 ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT BINDING 206 206 ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
SQ SEQUENCE 377 AA; 41049 MW; 977C1551533246C4 CRC64;
MHVLVLGSGQ LARMMSLAGA PLNIQISAYD VGSGNVVHPL TQQVLGHGLE NAIEQVDAIT
AEFEHIPHDV LDICELSGKF LPSTAAIKAG GDRRVEKALL DNAGVRNAKH YVIETREDFE
RAIEHVGIPM VLKSALGGYD GKGQWRLKEA AQIETIWAEM AECIAATPTQ AIVAEEFVPF
NREVSLVGAR GKDGSVEVYP LAENVHTNGV LSLSTAIDAP ELQAQAKQMF TAVADSLNYV
GVLALEFFDV EGTLLVNEIA PRVHNSGHWT QQGAETCQFE NHLRAVCGLP LGSTKLIRET
SMVNILGEDT LPEALLAMDG CHIHWYGKEK REGRKMGHIN VCGDYPGELH RRLCALAEVL
DPMIFPAVHE FAKQAQR
//
